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• W2894740570 abstract "Transient receptor potential mucolipin 1 (TRPML1), a lysosomal channel, maintains the low pH and calcium levels for lysosomal function. Several small molecules modulate TRPML1 activity. ML-SA1, a synthetic agonist, binds to the pore region and phosphatidylinositol-3,5-bisphosphate (PtdIns(3,5)P2), a natural lipid, stimulates channel activity to a lesser extent than ML-SA1; moreover, PtdIns(4,5)P2, another natural lipid, prevents TRPML1-mediated calcium release. Notably, PtdIns(3,5)P2 and ML-SA1 cooperate further increasing calcium efflux. Here we report the structures of human TRPML1 at pH 5.0 with PtdIns(3,5)P2, PtdIns(4,5)P2, or ML-SA1 and PtdIns(3,5)P2, revealing a unique lipid-binding site. PtdIns(3,5)P2 and PtdIns(4,5)P2 bind to the extended helices of S1, S2, and S3. The phosphate group of PtdIns(3,5)P2 induces Y355 to form a π-cation interaction with R403, moving the S4-S5 linker, thus allosterically activating the channel. Our structures and electrophysiological characterizations reveal an allosteric site and provide molecular insight into how lipids regulate TRP channels." @default.
• W2894740570 created "2018-10-12" @default.
• W2894740570 creator A5029362427 @default.
• W2894740570 creator A5059846691 @default.
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• W2894740570 date "2018-10-10" @default.
• W2894740570 modified "2023-10-17" @default.
• W2894740570 title "Structural basis for PtdInsP2-mediated human TRPML1 regulation" @default.
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• W2894740570 doi "https://doi.org/10.1038/s41467-018-06493-7" @default.
• W2894740570 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6180102" @default.
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• W2894740570 hasPublicationYear "2018" @default.
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